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| | ==Crystal Structure of Human BinCARD CARD, double mutant F16M/L66M SeMet form== | | ==Crystal Structure of Human BinCARD CARD, double mutant F16M/L66M SeMet form== |
| - | <StructureSection load='4fh0' size='340' side='right' caption='[[4fh0]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='4fh0' size='340' side='right'caption='[[4fh0]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fh0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FH0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fh0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FH0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dwn|4dwn]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh0 OCA], [https://pdbe.org/4fh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fh0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fh0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C9orf89 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fh0 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BINCA_HUMAN BINCA_HUMAN]] Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner. | + | [https://www.uniprot.org/uniprot/CAR19_HUMAN CAR19_HUMAN] Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner.<ref>PMID:15637807</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4fh0" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Chen, K E]] | + | [[Category: Large Structures]] |
| - | [[Category: Kobe, B]] | + | [[Category: Chen K-E]] |
| - | [[Category: Martin, J L]] | + | [[Category: Kobe B]] |
| - | [[Category: Apoptosis]] | + | [[Category: Martin JL]] |
| - | [[Category: Bcl10]]
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| - | [[Category: Er]]
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| - | [[Category: Immune system]]
| + | |
| - | [[Category: Mainly alpha]]
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| - | [[Category: Mitochondria]]
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| - | [[Category: Nucleus]]
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| Structural highlights
Function
CAR19_HUMAN Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner.[1]
Publication Abstract from PubMed
The caspase recruitment domain (CARD) is present in death-domain superfamily proteins involved in inflammation and apoptosis. BinCARD is named for its ability to interact with Bcl10 and inhibit downstream signalling. Human BinCARD is expressed as two isoforms that encode the same N-terminal CARD region but which differ considerably in their C-termini. Both isoforms are expressed in immune cells, although BinCARD-2 is much more highly expressed. Crystals of the CARD fold common to both had low symmetry (space group P1). Molecular replacement was unsuccessful in this low-symmetry space group and, as the construct contains no methionines, first one and then two residues were engineered to methionine for MAD phasing. The double-methionine variant was produced as a selenomethionine derivative, which was crystallized and the structure was solved using data measured at two wavelengths. The crystal structures of the native and selenomethionine double mutant were refined to high resolution (1.58 and 1.40 A resolution, respectively), revealing the presence of a cis-peptide bond between Tyr39 and Pro40. Unexpectedly, the native crystal structure revealed that all three cysteines were oxidized. The mitochondrial localization of BinCARD-2 and the susceptibility of its CARD region to redox modification points to the intriguing possibility of a redox-regulatory role.
The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized.,Chen KE, Richards AA, Caradoc-Davies TT, Vajjhala PR, Robin G, Lua LH, Hill JM, Schroder K, Sweet MJ, Kellie S, Kobe B, Martin J Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):774-84. doi:, 10.1107/S0907444913001558. Epub 2013 Apr 11. PMID:23633586[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Woo HN, Hong GS, Jun JI, Cho DH, Choi HW, Lee HJ, Chung CW, Kim IK, Jo DG, Pyo JO, Bertin J, Jung YK. Inhibition of Bcl10-mediated activation of NF-kappa B by BinCARD, a Bcl10-interacting CARD protein. FEBS Lett. 2004 Dec 17;578(3):239-44. doi: 10.1016/j.febslet.2004.10.094. PMID:15637807 doi:http://dx.doi.org/10.1016/j.febslet.2004.10.094
- ↑ Chen KE, Richards AA, Caradoc-Davies TT, Vajjhala PR, Robin G, Lua LH, Hill JM, Schroder K, Sweet MJ, Kellie S, Kobe B, Martin J. The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized. Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):774-84. doi:, 10.1107/S0907444913001558. Epub 2013 Apr 11. PMID:23633586 doi:10.1107/S0907444913001558
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